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- OJIMA TAKAO
- Graduate School of Fisheries Sciences, Hokkaido University
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- HIGUCHI TOMOYUKI
- Graduate School of Fisheries Sciences, Hokkaido University
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- NISHITA KIYOYOSHI
- Graduate School of Fisheries Sciences, Hokkaido University
この論文をさがす
説明
Heat-induced unfolding manner of light meromyosin (LMM) prepared from walleye pollack Theragra chalcogramma was investigated by circular dichroism spectrometry and α-chymotryptic digestion. α-Helix content of the LMM was originally 88% at 5°C, but decreased to 15% by increasing the temperature to 50°C. α-Chymotryptic digestion of the LMM and subsequent amino acid sequencing of the digests showed that unfolding of the LMM initiated in C-terminal region and progressed toward N-terminal region. When the LMM was digested with α-chymotrypsin after heat-treated at 50°C for 5min, the 42-kDa fragment corresponding to N-terminal approximately 2/3 region of the LMM and many smaller peptide fragments derived from remaining C-terminal 1/3 region were produced. These results indicate that the N-terminal 2/3 and C-terminal 1/3 regions of the LMM reversibly and irreversibly unfolding regions, respectively, upon heating.
収録刊行物
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- Fisheries science
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Fisheries science 68 (sup2), 1507-1510, 2002
公益社団法人 日本水産学会
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詳細情報 詳細情報について
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- CRID
- 1390001204429831552
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- NII論文ID
- 130003903863
- 40005648212
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- NII書誌ID
- AA10993718
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- NDL書誌ID
- 6423971
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- ISSN
- 09199268
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- 抄録ライセンスフラグ
- 使用不可